Antibodies were the ﬁrst elements of the immune system to be identiﬁed. They are antigen-reactive proteins present in an immune serum, called antiserum, and obtained after exposure of the vertebrate host to a given antigen, called an immunogen. By contrast, normal serum, also called preimmune serum, does not contain antibodies speciﬁc for that antigen. Antibodies belong to a group of proteins called immunoglobulins (Ig) that are present in the blood of immunized animals. The removal of cells and fibrin from blood is used to collect the serum fraction frequently referred to as antiserum. Listed in order of decreasing quantity found in plasma or serum, immunoglobulins comprise five major classes: immunoglobulin g (Igg), Iga, IgM, Igd and Ige. Each is composed of two identical heavy chains (H) and two identical light chains (L). The H chains differ in antigenic and structural properties, and determine the class and subclass of the molecule.

Insulin antibodies may be found in non-diabetic individuals complaining of hypoglycemic attacks. In this setting their presence can be an indicator of "factitious hypoglycemia" due to the surreptitious injection of insulin. Insulin autoantibodies in non-diabetic subjects can occasionally develop without exposure to exogenous insulin and may rarely become a cause of episodic hypoglycemia. Interaction of these antibodies with insulin autoantibodies could displace bound insulin from the insulin autoantibodies, resulting in hypoglycemia. Antibodies to exogenously delivered insulin are common with insulin treatment but are not often clinically significant. The development of antibodies depends on the purity, molecular structure, and storage conditions of the insulin administered as well as patient factors such as age, HLA type, and delivery route. Radio ligand binding (RLB) assays are the most common assay used for measurement of insulin antibodies.

Polyclonal antibodies (pAbs) are antibodies that are secreted by different B cell lineages within the body (whereas monoclonal antibodies come from a single cell lineage). They are a collection of immunoglobulin molecules that react against a specific antigen, each identifying a different epitope. These antibodies are typically produced by inoculation of a suitable mammal, such as a mouse, rabbit or goat. Larger mammals are often preferred as the amount of serum that can be collected is greater. An antigen is injected into the mammal. This induces the B-lymphocytes to produce IgG immunoglobulins specific for the antigen. This polyclonal IgG is purified from the mammal’s serum.

Hepatitis is an inflammation of your liver, often caused by an infection. About 95 percent of hepatitis infections are caused by one of five viruses: hepatitis A, B, C, D, or E and the symptoms of all of these infections are similar. Immune system makes IgM antibodies when you are first infected with HAV. It can take 14 to 50 days to develop symptoms of hepatitis A after you become infected. IgM antibodies usually begin to appear in your blood five to 10 days before you start having symptoms and can stay in your blood for about six months after the infection. Autoimmune hepatitis is a chronic inflammatory disease in which the immune system attacks healthy liver cells causing damage to the organ. There are three types of autoimmune hepatitis based upon the presence of antibodies in the blood.
Type 1 have antinuclear and smooth muscle antibodies
Type 2 show liver-kidney-microsomal antibodies
Type 3 (is currently not regarded as a clinically distinct AIH subgroup) display SLA/LP antibodies.
Autoimmune hepatitis is a chronic hepatitis characterized by immunologic and auto immunologic features, generally including the presence of circulating autoantibodies and a high total serum gamma globulin, usually confined to the IgG fraction [1]. Most cases respond to anti-inflammatory or immunosuppressive therapy. The main circulating autoantibodies, although not specific for the disease, are antinuclear antibodies (ANA) and anti-smooth muscle antibodies (ASMA) in type 1 disease and, in type 2 autoimmune hepatitis, anti-liver-kidney microsome-1 antibodies (ALKM-1) and anti-liver cytosol antibody-1 (ALC-1).

Different immunoglobulins can differ structurally; they all are built from the same basic units. Heavy and Light Chains, Heavy and Light Chains, Variable (V) and Constant (C) Regions, Hinge Region, Domains, Oligosaccharides. Immunoglobulin fragments produced by proteolytic digestion have proven very useful in elucidating structure/function relationships in immunoglobulins.

An autoantibody is an antibody (a type of protein) produced by the immune system that is directed against one or more of the individual's own proteins. Normally, the immune system is able to recognize and ignore the body's own healthy proteins, cells, and tissues, and to not overreact to non-threatening substances in the environment, such as foods. The immune system ceases to recognize one or more of the body's normal constituents as "self," leading to production of pathological auto antibodies. These auto antibodies attack the body's own healthy cells, tissues, and/or organs, causing inflammation and damage. Autoantibody tests may be ordered as part of an investigation of chronic progressive arthritis type symptoms and/or unexplained fevers, fatigue, muscle weakness and rashes. The Antinuclear antibody (ANA) test is often ordered first. ANA is a marker of the autoimmune process – it is positive with a variety of different autoimmune diseases but not specific. Antibody Profiling is used for identifying persons from forensic samples. The technology can uniquely identify a person by analyzing the antibodies in body fluids. A unique, individual set of antibodies, called individual specific auto antibodies (ISA) is found in blood, serum, saliva, urine, semen, perspiration, tears, and body tissues, and the antibodies are not affected by illness, medication, or food/drug intake.

Myeloperoxidase (MPO) is a peroxidase enzyme that in humans is encoded by the MPO gene on chromosome 17. MPO is a member of the XPO subfamily of peroxidases and produces hypochlorous acid (HOCl) from hydrogen peroxide (H2O2) and chloride anion (Cl−) (or the equivalent from a non-chlorine halide) during the neutrophil's respiratory burst. It requires heme as a cofactor. Antibodies against MPO have been implicated in various types of vasculitis, most prominently three clinically and pathologically recognized forms: granulomatosis with polyangiitis (GPA, formerly Wegener's granulomatosis), microscopic polyangiitis (MPA); and eosinophilic granulomatosis with polyangiitis (EGPA, formerly Churg–Strauss syndrome). Antibodies are also known as anti-neutrophil cytoplasmic antibodies (ANCAs), though ANCAs have also been detected in staining of the perinuclear region. Immunohistochemical staining for myeloperoxidase used to be administered in the diagnosis of acute myeloid leukemia to demonstrate that the leukemic cells were derived from the myeloid lineage.

Blood types are either A, B, AB, or O, and Rh positive or negative. A pregnant woman should know her blood type. This is because both the mother and her baby may experience problems if their blood types are different from each other, or if the mother has antibodies (antiglobulins) that react with antigens (proteins or factors) on the fetus' red blood cells. This may result in a serious condition referred to as Hemolytic Disease of the Newborn (HDN). The best known example is when an Rh-negative woman is pregnant with an Rh-positive baby. The woman's immune system can develop an antibody that attaches to the Rh-positive antigens on her fetus' red blood cells and target them for destruction. Although the first Rh-positive baby is unlikely to become ill, the antibodies produced during that first pregnancy will affect future Rh-positive babies. An antibody screen during the first trimester determines if potentially harmful antibodies are already present in the mother's blood. If a harmful antibody is detected, the baby's father should be tested, if possible, to see if his blood has antigens that react with the mother's antibody. If it does react, then the fetus' may also. If the antibody could react with the fetus', the health care provider should monitor the mother's antibody level and the fetus for the duration of the pregnancy.

Each antibody is specifically selected after binding to a certain antigen because of random somatic diversification in the antibody complementarity determining regions. A common analogy used to describe this is the fit between a lock and a key. An antigen (Ag) is any structural substance that serves as a target for the receptors of an adaptive immune response, TCR or BCR or its secreted form antibody. The antigen may originate from within the body ("self-antigen") or from the external environment ("non-self"). The immune system usually does not react to self-antigens under normal homeostatic conditions due to negative selection of T cells in the thymus and is supposed to identify and attack only "non-self" invaders from the outside world or modified/harmful substances present in the body under distressed conditions. Antigen presenting cells present antigens in the form of peptides on histocompatibility molecules. The T cells of the adaptive immune system recognize the antigens. Depending on the antigen and the type of the histocompatibility molecule, different types of T cells activate. For T-Cell Receptor (TCR) recognition, the peptide must be processed into small fragments inside the cell and presented by a major histocompatibility complex (MHC).

Antibody tests are done to find certain antibodies that attack red blood cells. Antibodies are proteins made by the immune system. Transfusion reaction Human blood is typed by certain markers (called antigens) on the surface of red blood cells camera.gif. If you get a blood transfusion, the transfused blood must match your type. Rh sensitization Rh is an antigen. The full name for this antigen is Rhesus factor. If a pregnant woman with Rh-negative blood is pregnant with a baby (fetus) with Rh-positive blood, Rh sensitization may occur. The baby may have Rh-positive blood if the father has Rh-positive blood. A type of hemolytic anemia called autoimmune hemolytic anemia is a rare disease that causes antibodies to be made against a person's own red blood cells. The direct Coombs test finds antibodies attached to your red blood cells. The antibodies may be those your body made because of disease or those you get in a blood transfusion. The indirect Coombs test finds certain antibodies that are in the liquid part of your blood (serum). These antibodies can attack red blood cells but are not attached to your red blood cells. The indirect Coombs test is commonly done to find antibodies in a recipient's or donor's blood before a transfusion.

Antibody-drug conjugates or ADCs are a new class of highly potent biopharmaceutical drugs designed as a targeted therapy for the treatment of people with cancer. By combining the unique targeting capabilities of monoclonal antibodies with the cancer-killing ability of cytotoxic drugs, antibody-drug conjugates allow sensitive discrimination between healthy and diseased tissue. This means that, in contrast to traditional chemotherapeutic agents, antibody-drug conjugates target and attack the cancer cell so that healthy cells are less severely affected. The biochemical reaction between the antibody and the target protein (antigen) triggers a signal in the tumor cell, which then absorbs or internalizes the antibody together with the cytotoxin. A stable link between the antibody and cytotoxic (anti-cancer) agent is a crucial aspect of an ADC. Linkers are based on chemical motifs including disulfides, hydrazones or peptides (cleavable), or thioethers (noncleavable) and control the distribution and delivery of the cytotoxic agent to the target cell. Cleavable and noncleavable types of linkers have been proven to be safe in preclinical and clinical trials.

Recombinant antibodies are highly specific detection probes in research, diagnostics, and have emerged over the last two decades as the fastest growing class of therapeutic proteins. Antibody generation has been dramatically accelerated by in vitro selection systems, particularly phage display. An increasing variety of recombinant production systems have been developed, ranging from Gram-negative and positive bacteria, yeasts and filamentous fungi, insect cell lines, mammalian cells to transgenic plants and animals. Currently, almost all therapeutic antibodies are still produced in mammalian cell lines in order to reduce the risk of immunogenicity due to altered, non-human glycosylation patterns.

Antibody engineering is a great tool for improving antibody functions and immunogenicity improvement. Engineered therapeutic antibodies are better for affinity maturation, specifically by improving on-rate of the antibody binding affinities. The need to overcome the immunogenicity problem of rodent antibodies in clinical practise has resulted in a plethora of strategies to isolate human antibodies. If human antibodies are to be used, then one would like to understand the basis by which different isotypes interact with host effector systems, and if possible, improve on nature by engineering in desirable modifications.

The evidence indicates that two simian immunodeficiency viruses (SIV), one from Chimpanzees (SIVcpz) and the other from sooty mangabeys (SIVsm), crossed the species barrier to humans, generating HIV-1 and HIV-2, respectively. The importance of characterizing the prevalence, geographic distribution, and genetic diversity of naturally occurring SIV infections to investigate whether humans continue to be exposed to SIV and if such exposure could lead to additional zoonotic transmissions. Through vigorous efforts made in the past two centuries, public health workers have succeeded in developing vaccines, antibiotics, and chemotherapeutics, and as a result most infectious diseases have been brought under control in industrialized countries. However, in developing countries, infectious diseases have been harder to contain, and the increase in migration and movement of populations in the last two decades has made national boundaries disappear as far as the transmission of infection is concerned. Some diseases, such as malaria, have been eradicated from industrialized countries mainly through extensive work on vector control, but their presence in developing countries has increased because of neglect or drug resistance. One of these proteases (Histidine Aspartic Protease, HAP) is homologous to three other aspartic proteases involved in hemoglobin metabolism but has a histidine in place of one of the two aspartic acids involved in catalysis. Despite this change, HAP is an active protease with distinct properties, and together with a series of cysteine and metalloproteases and a dipeptidyl peptidase, provides attractive focus for antimalarial drug development.

Auto-antibody is an antibody formed in response to, and reacting against, an antigenic constituent of the individual's own tissues. Several mechanisms may trigger the production of autoantibodies: an antigen, formed during fetal development and then sequestered, may be released as a result of infection, chemical exposure or trauma, as occurs in autoimmune thyroiditis, sympathetic uveitis and aspermia; there may be disorders of immune regulatory or surveillance function; antibodies produced against certain streptococcal antigens during infection may cross-react with myocardial tissue, causing rheumatic heart disease, or with glomerular basement membrane, causing glomerulonephritis; and normal body proteins may be converted to auto-antigens by chemicals, infectious organisms, or therapeutic drugs.

Monoclonal antibodies are monospecific antibodies that are made by identical immune cells that are all clones of a unique parent cell, in contrast to polyclonal antibodies which are made from several different immune cells. Monoclonal antibodies have monovalent affinity, in that they bind to the same epitope. They can be made in large quantities in the laboratory and are a cornerstone of immunology. They are used to treat many diseases, including some types of cancer. They target various proteins that influence cell activity such as receptors or other proteins present on the surface of normal and cancer cells. The specificity of Monoclonal Antibodies allows it’s binding to cancerous cells by coupling a cytotoxic agent such as a strong radioactive which then seeks out to destroy the cancer cells while not harming the healthy ones.

Antibodies are used extensively as diagnostic tools in many different formats. The term applied for antibody based diagnostic tests is “immunoassay”. Antibody-based immunoassays are the most commonly used confirmatory diagnostic assays and is the fastest growing technologies for the analysis of biomolecules. Trends in antibody based diagnosis show advances in assay specificity, detection technologies and sensitivity. Sensitivity and specificity is ensured depending on whether or not the antigen to be quantified competes with labeled antigen for a limited number of antibody binding sites. Monoclonal antibodies are now widely used in all areas of biological and medical research as well as in clinical diagnostic tests and in therapy. This review concentrates on the clinical use of antibodies in therapy particularly with regard to the properties of the antibodies which seem most relevant to their usefulness. In-vitro tests using human effector systems and in-vivo animal models have demonstrated the importance of the antibody isotype and valency for antigen as well as the specificity of binding. With the appropriate choice of antibody, used either alone, or conjugated to radioisotopes, drugs or toxins, it is possible to specifically deplete subpopulations of cells both in-vitro and in-vivo. Such antibodies can be used for tumour therapy, and for immunosuppression in organ transplantation and in autoimmune disorders.

Antibody therapies are the most successful immunotherapy, treating a wide range of cancers. Antibodies are proteins produced by the immune system that bind to a target antigen on the cell surface. In normal physiology the immune system uses them to fight pathogens. Each antibody is specific to one or a few proteins. Those that bind to cancer antigens are used to treat cancer. Cell surface receptors are common targets for antibody therapies. Among the most promising approaches to activating therapeutic antitumor immunity is the blockade of immune checkpoints. Immune checkpoints refer to a plethora of inhibitory pathways hardwired into the immune system that are crucial for maintaining self-tolerance and modulating the duration and amplitude of physiological immune responses in peripheral tissues in order to minimize collateral tissue damage. It is now clear that tumors co-opt certain immune-checkpoint pathways as a major mechanism of immune resistance, particularly against T cells that are specific for tumor antigens. Because many of the immune checkpoints are initiated by ligand–receptor interactions, they can be readily blocked by antibodies or modulated by recombinant forms of ligands or receptors. Cytotoxic T-lymphocyte-associated antigen 4 (CTLA4) antibodies were the first of this class of immunetherapeutics to achieve US Food and Drug Administration (FDA) approval. Preliminary clinical findings with blockers of additional immune-checkpoint proteins, such as programmed cell death protein 1 (PD1), indicate broad and diverse opportunities to enhance antitumor immunity with the potential to produce durable clinical responses.

Biosimilars and biobetters industry is likely to become a lot more dynamic and strategic than we’ve seen with small molecule generics; there will begin to become a premium on flexibility and willingness to take chances in an ever-shifting competitive and regulatory environment. The approval of the first biosimilar in the US is expected to save the healthcare industry and patients $5.7 billion over the next decade. The US biosimilars market is expected to reach $2 billion by 2018 and with the first biosimilar approved recently in America, this is an exciting time for the biosimilar field with approval in the US expected to increase during the next ten years. The regulatory landscape is evolving rapidly so it is important to understand the developments in the biosimilar guideline framework and the cohesion in legislation between the US and Europe. Key factors driving market growth include patent expiries of key biological drugs, cost containment measures from governments, aging population, and supporting legislations. The recent establishment of regulatory guidelines for biosimilars in the US is expected to add further momentum to the growth of the global biosimilars market. Increasing pressure from governments and insurers for greater biologic competition, there exists an incredible opportunity for biosimilar producers to capitalise on what is set to become the fastest growing sector of the pharmaceutical industry. Advice from experts was clear; biosimilar companies need to focus on products that see IP [intellectual property] begin to expire beyond 2020, the so-called third wave of biosimilar opportunity.

Conventional anticancer therapeutics often suffer from lack of specificity, resulting in toxicities to normal healthy tissues and poor therapeutic index. Antibody-drug conjugates (ADCs) constitute a therapeutic modality in which a cytotoxic agent is chemically linked to an antibody (Ab) that recognizes a tumor-associated antigen. The basic strategy underlying ADC technology is to combine the target selectivity of mAbs with the potency of cytotoxic agents, such as certain natural products and synthetic molecules, with the goal of generating therapeutic drugs that are highly efficacious but also safe. The ADC platform currently includes a growing repertoire of cytotoxic payloads, linker technologies and conjugation methods. Two ADCs have recently received FDA approval and more than 30 are in clinical development. This meeting aims to highlight advances in ADC research, clinical development and regulatory perspectives. Topics will range from early phase research focused on development of novel linker-payload and conjugation chemistries to clinical concepts and development of biomarkers and patient selection strategies.

The outlook for therapeutic antibodies is very promising. This meeting will highlight current trends in development including identifying and validating novel targets, improving drug-like properties, employing immunotherapy approaches and advancing novel constructs. This program has consistently recruited top thought leaders in the field to review the status of myriad innovative antibodies and key ideas for advancing them towards the clinic. The immune system has evolved to fight infection, and the response to microbial infection involves the activation of a complex network in which numerous cell types, soluble factors and adhesion molecules of the host immune system participate. It is therefore not possible to produce a good textbook in immunology without any reference to infection or infectious agents. Immunology, Infection, and Immunity has been produced with this in mind, and the Editors have clearly done this with an appreciation of the immune system as a defence system. While the emphasis of the book is on immunity to infectious diseases, it also includes diseases that arise as a result of inactivity or hyperactivity on the part of the immune system. Immunodeficiency, hypersensitivity and autoimmunity are outcomes when the immune system fails to act or over-reacts.

Anticancer antibodies has created great interest in antibody-based therapeutics for hematopoietic malignant neoplasms and solid tumors. Given the likelihood of lower toxic effects of antibodies that target tumor cells and have limited impact on nonmalignant bystander organs vs small molecules, the potential increased efficacy by conjugation to radioisotopes and other cellular toxins, and the ability to characterize the target with clinical laboratory diagnostics to improve the drug's clinical performance, current and future antibody therapeutics are likely to find substantial roles alone and in combination therapeutic strategies for treating patients with cancer. Therapeutic antibodies have become a major strategy in clinical oncology owing to their ability to bind specifically to primary and metastatic cancer cells with high affinity and create antitumor effects by complement-mediated cytolysis and antibody-dependent, cell-mediated cytotoxicity (naked antibodies) or by the focused delivery of radiation or cellular toxins (conjugated antibodies). Novel antibody-based structures with multiple antigen-recognition sites, altered size or effector domains have been shown to influence the targeting ability of antibodies. This review will focus on novel approaches of antibody-based cancer therapy.

Cancer immunotherapy—treatments that harness and enhance the innate powers of the immune system to fight cancer—represents the most promising new cancer treatment approach since the development of the first chemotherapies in the late 1940s. Because of the immune system’s extraordinary power, its capacity for memory, its exquisite specificity, and its central and universal role in human biology, these treatments have the potential to achieve complete, long-lasting remissions and cancer cures, with few or no side effects, and for any cancer patient, regardless of their cancer type. Immunotherapy is treatment that uses your body's own immune system to help fight cancer. These treatment modalities are all based on destroying cancer cells by burning them (irradiation), poisoning them (chemotherapy) or removing them (surgery). While they can effectively kill or remove cancer cells, the use of these treatments often is limited because large numbers of healthy cells also tend to be destroyed. This often results in extreme morbidity and/or disfigurement of the patients treated with them. In the worst cases, these treatments can sometimes result in the patient's death. Immunotherapy is one of the more recent approaches to cancer therapy. It is based on the generally-accepted hypothesis that the immune system is the best tool humans have for fighting disease.

The first monoclonal antibodies were typically made entirely from mouse cells. One problem with this is that the human immune system will see these antibodies as foreign (because they’re from a different species) and will mount a response against them. In the short term, this can sometimes cause an immune response. In the long term, it means that the antibodies may only work the first time they are given; after that, the body’s immune system is primed to destroy them before they can provide treatment. This study presents a technology that generates stable, soluble, ultra-humanized antibodies via single-step CDR redundancy minimization. Lead clones demonstrated high stability, with affinity and specificity equivalent to, or better than, the parental immunoglobulin. This significantly lowered non-human sequence content, minimized t- and b-cell epitope risk in the final molecules and provided a heat map for the essential non-human CDR residue content of antibodies from disparate sources. Antibody humanization uses multiple sequence segments derived from variable (V) regions of unrelated human antibodies, unlike other technologies that typically use a single human V region framework as acceptors for complementarity determining regions (CDRs) from starting antibodies (typically rodent). Through careful selection of human sequence segments and the application of in silico tools, CD4+ T cell epitopes are avoided so the risk of immunogenicity is reduced compared to standard humanized antibodies whilst antibody affinity and specificity is maintained. Immunogenicity assessment technology is used to confirm T cell epitopes have been removed. We can provide small quantities of antibody for research purposes using either transient expression systems or through generating research-grade stable cell lines. For larger quantities for development a stable high-expressing manufacturing cell line can be established using our cell line development service and then transferred to a cGMP compliant manufacturer.

The development of cancer therapies is increasingly dependent on our understanding of tumor biology, and biomarkers—especially predictive biomarkers—are crucial tools in the field of personalized medicine and health economics, in particular, as they enable definition of the populations of patients who are most likely to benefit from targeted therapies. More-effective patient selection than is possible at present is mandatory to improve the success rate of new therapies, which are sometimes prohibitively expensive, and thereby increase their cost–utility; thus, delineating reliable predictive biomarkers is essential if we are to achieve this objective. One commonly used definition of a biomarker is a measurable indicator that is used to distinguish precisely, reproducibly and objectively either a normal biological state from a pathological state, or the response to a specific therapeutic intervention. In fact, biomarkers are used for numerous purposes: to predict survival (prognostic biomarkers); to assess drug safety and evaluate target engagement and the immediate consequence on biological processes (pharmacodynamics biomarkers), to identify patients who are more likely to benefit from a treatment (predictive biomarkers; more generally termed companion biomarkers when associated with a specific therapeutic agent); to predict outcome given the response to therapy (surrogate biomarkers); and to monitor disease progression or therapeutic efficacy (monitoring biomarkers). Identification and widespread use of biomarkers will help ensure that patients receive the best possible therapeutic strategies, thereby avoiding unnecessary treatments and associated toxicities, and eventually reducing total health costs. Even though immunotherapeutic approaches are being studied in many cancer types, correlative studies have thus far been most extensively conducted in melanoma, providing valuable experience and making it a model system for identifying therapeutic biomarkers.

Conferences Series invites all the participants from all over the world to attend “2nd International Conference and Exhibition on Antibodies” during July 11-12, 2016 in Philadelphia, USA which includes prompt keynote presentations, Oral talks, Poster presentations and Exhibitions.

Antibodies-2016 which aims to gather the most elegant societies and industries along with the renowned and honorable persons form top universities across the globe. Antibodies-2016 on behalf of its organizing Committee welcomes all the Immunology researchers, industrialists, young scientists as well as student and corporate delegates to participate and to have a great experience. The theme of the conference of Antibodies is based on The New Era of Antibody Research and Therapy. During Antibodies conferences, the International symposiums, B2B meetings, international workshops will also be organized to discuss the specific topics in the field of Immunology and Microbiology. The conference also welcomes International exhibitions form corporate sectors to showcase the recent advancements in tools and techniques. Conferences Series organizes a conference series of 1000+ Global Events inclusive of 300+ Conferences, 500+ Upcoming and Previous Symposiums and Workshops in USA, Europe & Asia with support from 1000 more scientific societies and publishes 700+ Open access journals which contains over 30000 eminent personalities, reputed scientists as editorial board members.

Why to attend???

With members from around the world focused on learning about antibodies and its advances; this is your best opportunity to reach the largest assemblage of participants from the Immunology community. Conduct presentations, distribute information, meet with current and potential scientists, make a splash with new drug developments, and receive name recognition at this 2-day event. World-renowned speakers, the most recent techniques, developments, and the newest updates in Antibodies Research are hallmarks of this conference.

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Antibodies Associations and Societies

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Manufacturing Medical Devices Companies

Monoclonal antibodies (Antibody drugs) are now used for treatment of a wide array of diseases, especially cancer, autoimmune, and inflammatory diseases. The development of these new molecular agents, successfully directed to specific cellular targets, is expected to play an increasingly important role in future clinical protocol, and perhaps finally provide a means to achieve long-term tolerance in human allograft recipients.

Large scale research development is being conducted in the field of antibody drugs for the past two decades. By 2009, approximately 30 new antibody drugs were launched in the market. With an intention of launching new blockbuster drugs and to reform the pharmaceuticals industry, large pharmaceutical companies have begun to undertake aggressive steps to enter this market. Hence, it is expected that the antibody drugs segment will experience impressive growth in the global pharmaceuticals market. For instance, the global market for therapeutic monoclonal antibodies (mAbs) was estimated at US$44.6 billion in 2011. The global mAb market is expected to rise at a compound annual growth rate (CAGR) of 5.3% to nearly $58 billion in 2016 and is predicted to have a double digit growth of around 15% from the year 2012 to 2018. One of the key factors contributing to this market growth is the increasing prevalence of cancer. The Global Monoclonal Antibodies market has also been witnessing the trend of the increasing use of monoclonal antibodies in the development of personalized medicines. Technological enhancements and huge R&D in genomic studies have propelled the growth of this market.

Globally, North America is viewed as the largest market for antibody drugs followed by Europe. However, infrastructural development in the healthcare system and growth in awareness regarding the treatment of chronic diseases may influence a rapid growth of this market in Asia and in other parts of the world.

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